Evidence map›Paper›PMID 26919668›Full record

ArticlePloS one2016

Differential Subplastidial Localization and Turnover of Enzymes Involved in Isoprenoid Biosynthesis in Chloroplasts.

Catalina Perello, Ernesto Llamas, Vincent Burlat, Miriam Ortiz-Alcaide, Michael A Phillips, Pablo Pulido, Manuel Rodriguez-Concepcion

Erratum issuedOpen access · goldAbstract readComparative Study
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
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  13. Frontiers in plant science · 2021
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  14. Article
  15. Cellular and Subcellular Compartmentation of the 2Plants (Basel, Switzerland) · 2020
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Catalina PerelloProgram of Plant Metabolism and Metabolic Engineering, Centre for Research in Agricultural Genomics (CRAG) CSIC-IRTA-UAB-UB, Campus UAB Bellaterra, 08193 Barcelona, Spain.
Ernesto LlamasProgram of Plant Metabolism and Metabolic Engineering, Centre for Research in Agricultural Genomics (CRAG) CSIC-IRTA-UAB-UB, Campus UAB Bellaterra, 08193 Barcelona, Spain.
Vincent BurlatUniversité de Toulouse, CNRS, UMR 5546, BP 42617 Auzeville, 31326 Castanet-Tolosan, France.
Miriam Ortiz-AlcaideProgram of Plant Metabolism and Metabolic Engineering, Centre for Research in Agricultural Genomics (CRAG) CSIC-IRTA-UAB-UB, Campus UAB Bellaterra, 08193 Barcelona, Spain.
Michael A PhillipsProgram of Plant Metabolism and Metabolic Engineering, Centre for Research in Agricultural Genomics (CRAG) CSIC-IRTA-UAB-UB, Campus UAB Bellaterra, 08193 Barcelona, Spain.
Pablo PulidoProgram of Plant Metabolism and Metabolic Engineering, Centre for Research in Agricultural Genomics (CRAG) CSIC-IRTA-UAB-UB, Campus UAB Bellaterra, 08193 Barcelona, Spain.
Manuel Rodriguez-ConcepcionProgram of Plant Metabolism and Metabolic Engineering, Centre for Research in Agricultural Genomics (CRAG) CSIC-IRTA-UAB-UB, Campus UAB Bellaterra, 08193 Barcelona, Spain.
Center for Research in Agricultural Genomics · ESUniversité de Toulouse · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plastidial isoprenoids are a diverse group of metabolites with roles in photosynthesis, growth regulation, and interaction with the environment. The methylerythritol 4-phosphate (MEP) pathway produces the metabolic precursors of all types of plastidial isoprenoids. Proteomics studies in Arabidopsis thaliana have shown that all the enzymes of the MEP pathway are localized in the plastid stroma. However, immunoblot analysis of chloroplast subfractions showed that the first two enzymes of the pathway, deoxyxylulose 5-phosphate synthase (DXS) and reductoisomerase (DXR), can also be found in non-stromal fractions. Both transient and stable expression of GFP-tagged DXS and DXR proteins confirmed the presence of the fusion proteins in distinct subplastidial compartments. In particular, DXR-GFP was found to accumulate in relatively large vesicles that could eventually be released from chloroplasts, presumably to be degraded by an autophagy-independent process. Together, we propose that protein-specific mechanisms control the localization and turnover of the first two enzymes of the MEP pathway in Arabidopsis chloroplasts.

Indexed as

Agrobacterium tumefaciensAldose-Ketose IsomerasesArabidopsisArabidopsis ProteinsChloroplastsGenes, ReporterGenetic VectorsNicotianaPlant LeavesPlants, Genetically ModifiedProtein AggregatesProtein TransportRecombinant Fusion ProteinsSubcellular FractionsTerpenesThylakoid Membrane Proteins1-deoxy-D-xylulose 5-phosphate reductoisomeraseAldose-Ketose IsomerasesArabidopsis Proteinsdeoxyxylulose-5-phosphate synthaseProtein AggregatesRecombinant Fusion ProteinsTerpenesThylakoid Membrane ProteinsTransferases

Identifiers

PMID26919668
PMCPMC4769067
OpenAlexW2286256939

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.